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Database: UniProt
Entry: A0A385BUY7_9FLAO
LinkDB: A0A385BUY7_9FLAO
Original site: A0A385BUY7_9FLAO 
ID   A0A385BUY7_9FLAO        Unreviewed;       169 AA.
AC   A0A385BUY7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC {ECO:0000256|ARBA:ARBA00020092};
DE            EC=3.1.3.45 {ECO:0000256|ARBA:ARBA00013066};
DE   AltName: Full=KDO 8-P phosphatase {ECO:0000256|ARBA:ARBA00031051};
GN   ORFNames=CJ739_3892 {ECO:0000313|EMBL:AXP82951.1};
OS   Mariniflexile sp. TRM1-10.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Mariniflexile.
OX   NCBI_TaxID=2027857 {ECO:0000313|EMBL:AXP82951.1, ECO:0000313|Proteomes:UP000259852};
RN   [1] {ECO:0000313|Proteomes:UP000259852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRM1-10 {ECO:0000313|Proteomes:UP000259852};
RA   Kim J.F., Kwak M.-J.;
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-
CC         deoxy-alpha-D-manno-oct-2-ulosonate + phosphate;
CC         Xref=Rhea:RHEA:11500, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:85985, ChEBI:CHEBI:85986; EC=3.1.3.45;
CC         Evidence={ECO:0000256|ARBA:ARBA00000898};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRSR:PIRSR006118-2};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the KdsC family.
CC       {ECO:0000256|ARBA:ARBA00005893}.
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DR   EMBL; CP022985; AXP82951.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A385BUY7; -.
DR   KEGG; marf:CJ739_3892; -.
DR   OrthoDB; 9805604at2; -.
DR   Proteomes; UP000259852; Chromosome.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR010023; KdsC_fam.
DR   NCBIfam; TIGR01662; HAD-SF-IIIA; 1.
DR   NCBIfam; TIGR01670; KdsC-phosphatas; 1.
DR   PANTHER; PTHR21485:SF5; 3-DEOXY-D-MANNO-OCTULOSONATE 8-PHOSPHATE PHOSPHATASE KDSC; 1.
DR   PANTHER; PTHR21485; HAD SUPERFAMILY MEMBERS CMAS AND KDSC; 1.
DR   Pfam; PF08282; Hydrolase_3; 1.
DR   PIRSF; PIRSF006118; KDO8-P_Ptase; 1.
DR   SFLD; SFLDG01138; C1.6.2:_Deoxy-d-mannose-octulo; 1.
DR   SFLD; SFLDG01136; C1.6:_Phosphoserine_Phosphatas; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR006118-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR006118-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000259852}.
FT   BINDING         19
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT   BINDING         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
FT   BINDING         112
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006118-2"
SQ   SEQUENCE   169 AA;  18385 MW;  09ECADF1A312B8D6 CRC64;
     MEEKSYKEYL NHITTFIFDV DGVLTDGTVL VTTSGELLRT MGIKDGYALK FAVSAGYNVA
     IISAGTNEGV KLRLEGLGVK DVFLGAHDKV KQFEAYIKAN NIKSENILYM GDDVADYPVM
     KLVGLPSCPQ DAIPEVKGIA KYISHKKGGE GAARDVIEQV LKVQGKWAL
//
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